Effect of AOT on enzymatic activity of the organic solvent resistant tyrosinase from Streptomyces sp. REN-21 in aqueous solutions and water-in-oil microemulsions

Rodakiewicz-Nowak, Janina; Ito, Masaaki

doi:10.1016/j.jcis.2004.10.052

Cited by 17 publications

(8 citation statements)

References 23 publications

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“…At higher surfactant concentrations, the reversed micelles collide more frequently as their large population. As a result, the diffusion and exchange of the molecules in the system are enhanced [3,29].…”

Section: Effects Of the Surfactant Concentration On The Substrate Dismentioning

confidence: 99%

Effects of surfactants on enzyme-containing reversed micellar system

et al. 2011

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With the development of colloid interface and enzyme technologies, enzyme-containing reversed micellar system has been receiving much attention in bioseparation and bioconversion. Because of its high efficiency, it has brought new opportunities for the development of molecular biotechnology. Reversed micelles represent nano-sized aqueous droplets stabilized by surfactant amphiphiles inside the bulk organic solvents. The entrapped enzymes have enhanced activities under those conditions as suited in the lipid bilayers of biological membranes. The fundamentals of enzyme-containing reversed micellar system are described in this paper, with special emphasis on the effects of surfactants varying in concentrations and structures. The latest study progress on the surfactants application in enzyme-containing reversed micelles is reviewed. The introduction of novel functional surfactants in micellar enzymology and their future development are also discussed. reversed micelle, enzyme, surfactant concentration, surfactant molecular structure, enzyme-containing reversed micellar system.

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Section: Effects Of the Surfactant Concentration On The Substrate Dismentioning

confidence: 99%

Effects of surfactants on enzyme-containing reversed micellar system

et al. 2011

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“…As a result, the use of microemulsions for the extension of their applications is essential. Rodakiewicz-Nowak et al [87] demonstrated that yellow lacasse from Pleurotus ostreatus in isooctane/AOT/water microemulsions retained its catalytic activity, however, it was markedly reduced in comparison to that obtained in aqueous solution. This observation was extensively investigated with respect to the microemulsion's w o and the conclusion was that w o versus the oxidation rates for both yellow laccases and blue laccases have a linear dependence [88].…”

Section: Laccasesmentioning

confidence: 99%

“…Laccase is a phenoloxidase that was also solubilized in W/IL microemulsions showing a higher catalytic activity when compared to aqueous solution [87]. Xue et al [90] constructed a W/IL microemulsion consisting of [BMIM][PF6]/AOT/Triton X-100/water and studied the activity of laccase.…”

Section: Laccasesmentioning

confidence: 99%

“…In AOT microemulsions enzymatic activity shows a peak on the increase of temperature, whereas in CTAB microemulsions there is no optimum found [95]. Rodakiewicz-Nowak et al [87] investigated the oxidation of 4-t-butylcatechol by tyrosinase in the same system and showed that w o affected the enzyme activity, with the enzyme being active in highly concentrated AOT microemulsions even at a low water content. Nevertheless, the effect of water content of the microemulsion towards the initial rate of the reaction did not demonstrate a bell-shaped dependence, but showed an increase followed by a plateau.…”

Section: Tyrosinasementioning

confidence: 99%

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Oxidation Catalysis by Enzymes in Microemulsions

2017

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Microemulsions are regarded as "the ultimate enzyme microreactors" for liquid oxidations. Their structure, composed of water nanodroplets dispersed in a non-polar medium, provides several benefits for their use as media for enzymatic transformations. They have the ability to overcome the solubility limitations of hydrophobic substrates, enhance the enzymatic activity (superactivity phenomenon) and stability, while providing an interface for surface-active enzymes. Of particular interest is the use of such systems to study biotransformations catalyzed by oxidative enzymes. Nanodispersed biocatalytic media are perfect hosts for liquid oxidation reactions catalyzed by many enzymes such as heme peroxidases, phenoloxidases, cholesterol oxidase, and dehydrogenases. The system's composition and structural properties are important for better understanding of nanodispersion-biocatalyst interactions.

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“…BCME systems have been previously explored for drug delivery and shown to preserve the stability and enzymatic activity of protein [4,8,9,[11][12][13][14][15][16]. However, unlike reverse micellar microemulsions, encapsulation of biocolloids such as proteins in BCMEs has been explored to a much lesser extent [17][18][19][20][21][22]. Permeation and transport of proteins enabled by BCMEs has unique applications in the development of efficient surface formulations.…”

Section: Introductionmentioning

confidence: 99%